Q8WWW0 (RASF5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras association domain-containing protein 5

Alternative name(s):
New ras effector 1
Regulator for cell adhesion and polarization enriched in lymphoid tissues
Short name=RAPL

Gene names

Name:	RASSF5
Synonyms:	NORE1, RAPL

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	418 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Potential tumor suppressor. Seems to be involved in lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or chemokine stimulation to integrin activation. Isoform 2 stimulates lymphocyte polarization and the patch-like distribution of ITGAL/LFA-1, resulting in an enhanced adhesion to ICAM1. Together with RAP1A may participate in regulation of microtubule growth. The association of isoform 2 with activated RAP1A is required for directional movement of endothelial cells during wound healing. May be involved in regulation of Ras apoptotic function. The RASSF5-STK4/MST1 complex may mediate HRAS1 and KRAS induced apoptosis. Ref.2 Ref.9 Ref.11
Subunit structure	Interacts directly with activated HRAS1; a RASSF5-STK4/MST1 complex probably associates with activated HRAS1. Interacts with KRAS. Probably interacts with Ras-like GTPases RRAS, RRAS2, MRAS, RAP1B, RAP2A and RALA. Can self-associate. Interacts with RSSF1 isoform A. The RSSF1 isoform A-RSSF5 heterodimer probably mediates the association of RSSF1 with HRAS1 By similarity. Isoform 2 interacts with activated RAP1A and ITGAL/LFA-1. Binds STK4/MST1, inhibiting STK4/MST1 autoactivation. Ref.2 Ref.10 Ref.11
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton. Note: Isoform 2 is mainly located in the perinuclear region of unstimulated primary T-cells. Upon stimulation translocates to the leading edge and colocalizes with ITGAL/LFA-1 in the peripheral zone of the immunological synapse. Isoform 2 is localized to growing microtubules in vascular endothelial cells and is dissociated from microtubules by activated RAP1A. Ref.2 Ref.11
Tissue specificity	Widely expressed. Frequently down-regulated in lung tumor cell lines and primary lung tumors. Ref.1 Ref.9
Sequence similarities	Contains 1 phorbol-ester/DAG-type zinc finger. Contains 1 Ras-associating domain. Contains 1 SARAH domain.
Caution	Was termed (Ref.3) RASSF3.
Sequence caution	The sequence AAH04270.1 differs from that shown. Reason: Erroneous initiation. The sequence AAH07203.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Cytoplasm Cytoskeleton Microtubule
Coding sequence diversity	Alternative splicing
Disease	Tumor suppressor
Domain	Zinc-finger
Ligand	Metal-binding Zinc
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW intracellular signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GABARAP	O95166	2	EBI-367390,EBI-712001
GABARAPL1	Q9H0R8	2	EBI-367390,EBI-746969
GABARAPL2	P60520	2	EBI-367390,EBI-720116
MAP1LC3B	Q9GZQ8	5	EBI-367390,EBI-373144
MAP1LC3C	Q9BXW4	2	EBI-367390,EBI-2603996
RAP1A	P62834	3	EBI-960502,EBI-491414
STK3	Q13188	3	EBI-367390,EBI-992580
STK4	Q13043	4	EBI-960502,EBI-367376

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8WWW0-1)

Also known as: A; NORE1A;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8WWW0-2)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     1-153: Missing.
     154-193: CKFTCHPECR...ESTLTVTFSQ → MTVDSSMSSG...RNAQSKHLSK

Note: Initiator Met-1 is removed. Contains a N-acetylthreonine at position 2.

Isoform 3 (identifier: Q8WWW0-3)

Also known as: C; NORE1B;

The sequence of this isoform differs from the canonical sequence as follows:
     331-336: LFQKLS → GCLLHP
     337-418: Missing.

Isoform 4 (identifier: Q8WWW0-4)

Also known as: D;

The sequence of this isoform differs from the canonical sequence as follows:
     382-418: TILEKEEQDKIQQVQKKYDKFRQKLEEALRESQGKPG → SSWCIQIYLYY

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 418	418	Ras association domain-containing protein 5		PRO_0000240401
Regions
	Domain	274 – 364	91	Ras-associating
	Domain	366 – 413	48	SARAH
	Zinc finger	122 – 170	49	Phorbol-ester/DAG-type
Amino acid modifications
	Modified residue	352	1	Phosphothreonine Ref.12 Ref.13
Natural variations
	Alternative sequence	1 – 153	153	Missing in isoform 2.		VSP_019363
	Alternative sequence	154 – 193	40	CKFTC…VTFSQ → MTVDSSMSSGYCSLDEELED CFFTAKTTFFRNAQSKHLSK in isoform 2.		VSP_019364
	Alternative sequence	331 – 336	6	LFQKLS → GCLLHP in isoform 3.		VSP_019365
	Alternative sequence	337 – 418	82	Missing in isoform 3.		VSP_019366
	Alternative sequence	382 – 418	37	TILEK…QGKPG → SSWCIQIYLYY in isoform 4.		VSP_019367

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (A) (NORE1A) [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 4AFBC69B1325CC9E	FASTA	418	47,090
	10 20 30 40 50 60 MAMASPAIGQ RPYPLLLDPE PPRYLQSLSG PELPPPPPDR SSRLCVPAPL STAPGAREGR 70 80 90 100 110 120 SARRAARGNL EPPPRASRPA RPLRPGLQQR LRRRPGAPRP RDVRSIFEQP QDPRVPAERG 130 140 150 160 170 180 EGHCFAELVL PGGPGWCDLC GREVLRQALR CTNCKFTCHP ECRSLIQLDC SQQEGLSRDR 190 200 210 220 230 240 PSPESTLTVT FSQNVCKPVE ETQRPPTLQE IKQKIDSYNT REKNCLGMKL SEDGTYTGFI 250 260 270 280 290 300 KVHLKLRRPV TVPAGIRPQS IYDAIKEVNL AATTDKRTSF YLPLDAIKQL HISSTTTVSE 310 320 330 340 350 360 VIQGLLKKFM VVDNPQKFAL FKRIHKDGQV LFQKLSIADR PLYLRLLAGP DTEVLSFVLK 370 380 390 400 410 ENETGEVEWD AFSIPELQNF LTILEKEEQD KIQQVQKKYD KFRQKLEEAL RESQGKPG
	Isoform 2 (B) [UniParc]. Checksum: 66AD5D84EFA6D6CB	FASTA	265	30,359
	10 20 30 40 50 60 MTVDSSMSSG YCSLDEELED CFFTAKTTFF RNAQSKHLSK NVCKPVEETQ RPPTLQEIKQ 70 80 90 100 110 120 KIDSYNTREK NCLGMKLSED GTYTGFIKVH LKLRRPVTVP AGIRPQSIYD AIKEVNLAAT 130 140 150 160 170 180 TDKRTSFYLP LDAIKQLHIS STTTVSEVIQ GLLKKFMVVD NPQKFALFKR IHKDGQVLFQ 190 200 210 220 230 240 KLSIADRPLY LRLLAGPDTE VLSFVLKENE TGEVEWDAFS IPELQNFLTI LEKEEQDKIQ 250 260 QVQKKYDKFR QKLEEALRES QGKPG
	Isoform 3 (C) (NORE1B) [UniParc]. Checksum: 2657B6DAECD8D6A9	FASTA	336	37,433
	10 20 30 40 50 60 MAMASPAIGQ RPYPLLLDPE PPRYLQSLSG PELPPPPPDR SSRLCVPAPL STAPGAREGR 70 80 90 100 110 120 SARRAARGNL EPPPRASRPA RPLRPGLQQR LRRRPGAPRP RDVRSIFEQP QDPRVPAERG 130 140 150 160 170 180 EGHCFAELVL PGGPGWCDLC GREVLRQALR CTNCKFTCHP ECRSLIQLDC SQQEGLSRDR 190 200 210 220 230 240 PSPESTLTVT FSQNVCKPVE ETQRPPTLQE IKQKIDSYNT REKNCLGMKL SEDGTYTGFI 250 260 270 280 290 300 KVHLKLRRPV TVPAGIRPQS IYDAIKEVNL AATTDKRTSF YLPLDAIKQL HISSTTTVSE 310 320 330 VIQGLLKKFM VVDNPQKFAL FKRIHKDGQV GCLLHP
	Isoform 4 (D) [UniParc]. Checksum: B0D8CF859F5757D7	FASTA	392	44,082
	10 20 30 40 50 60 MAMASPAIGQ RPYPLLLDPE PPRYLQSLSG PELPPPPPDR SSRLCVPAPL STAPGAREGR 70 80 90 100 110 120 SARRAARGNL EPPPRASRPA RPLRPGLQQR LRRRPGAPRP RDVRSIFEQP QDPRVPAERG 130 140 150 160 170 180 EGHCFAELVL PGGPGWCDLC GREVLRQALR CTNCKFTCHP ECRSLIQLDC SQQEGLSRDR 190 200 210 220 230 240 PSPESTLTVT FSQNVCKPVE ETQRPPTLQE IKQKIDSYNT REKNCLGMKL SEDGTYTGFI 250 260 270 280 290 300 KVHLKLRRPV TVPAGIRPQS IYDAIKEVNL AATTDKRTSF YLPLDAIKQL HISSTTTVSE 310 320 330 340 350 360 VIQGLLKKFM VVDNPQKFAL FKRIHKDGQV LFQKLSIADR PLYLRLLAGP DTEVLSFVLK 370 380 390 ENETGEVEWD AFSIPELQNF LSSWCIQIYL YY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"RASSF3 and NORE1: identification and cloning of two human homologues of the putative tumor suppressor gene RASSF1." Tommasi S., Dammann R., Jin S.-G., Zhang X.-F., Avruch J., Pfeifer G.P. Oncogene 21:2713-2720(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[2]	"RAPL, a Rap1-binding molecule that mediates Rap1-induced adhesion through spatial regulation of LFA-1." Katagiri K., Maeda A., Shimonaka M., Kinashi T. Nat. Immunol. 4:741-748(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION IN INTEGRIN ACTIVATION, INTERACTION WITH RAP1A AND ITGAL, SUBCELLULAR LOCATION.
[3]	"RASSF3 is regulated by methylation in lung and breast tumor cell lines." Burbee D.G., White M.A., Minna J.D. Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[5]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Lymph node.
[6]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4). Tissue: Skin.
[9]	"The pro-apoptotic Ras effector Nore1 may serve as a Ras-regulated tumor suppressor in the lung." Vos M.D., Martinez A., Ellis C.A., Vallecorsa T., Clark G.J. J. Biol. Chem. 278:21938-21943(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A TUMOR SUPPRESSOR, TISSUE SPECIFICITY.
[10]	"Regulation of the MST1 kinase by autophosphorylation, by the growth inhibitory proteins, RASSF1 and NORE1, and by Ras." Praskova M., Khoklatchev A., Ortiz-Vega S., Avruch J. Biochem. J. 381:453-462(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH STK4/MST1.
[11]	"Local activation of Rap1 contributes to directional vascular endothelial cell migration accompanied by extension of microtubules on which RAPL, a Rap1-associating molecule, localizes." Fujita H., Fukuhara S., Sakurai A., Yamagishi A., Kamioka Y., Nakaoka Y., Masuda M., Mochizuki N. J. Biol. Chem. 280:5022-5031(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN MICROTUBULE GROWTH REGULATION, SUBCELLULAR LOCATION, INTERACTION WITH RAP1A.
[12]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-352, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-352, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE.
[14]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF445801 mRNA. Translation: AAL38592.1. AY261332 mRNA. Translation: AAP83360.1. AY062002 mRNA. Translation: AAL40388.1. AY062003 mRNA. Translation: AAL40389.1. AY216268 mRNA. Translation: AAO61668.1. AK289861 mRNA. Translation: BAF82550.1. AL832784 mRNA. Translation: CAI46164.1. AL591846, AL354681 Genomic DNA. Translation: CAI13536.1. AL591846, AL354681 Genomic DNA. Translation: CAI13538.1. AL354681, AL591846 Genomic DNA. Translation: CAI15252.1. AL591846, AL354681 Genomic DNA. Translation: CAI13537.1. AL591846, AL354681 Genomic DNA. Translation: CAI13542.1. AL354681, AL591846 Genomic DNA. Translation: CAI15253.1. AL354681, AL591846 Genomic DNA. Translation: CAI15254.1. AL354681, AL591846 Genomic DNA. Translation: CAI15256.1. CH471100 Genomic DNA. Translation: EAW93544.1. BC004270 mRNA. Translation: AAH04270.1. Different initiation. BC007203 mRNA. Translation: AAH07203.1. Different initiation. BC042651 mRNA. Translation: AAH42651.1.
IPI	IPI00103528. IPI00179101. IPI00183637. IPI00332633.
RefSeq	NP_872604.1. NM_182663.2. NP_872605.1. NM_182664.2. NP_872606.1. NM_182665.2.
UniGene	Hs.497579.
3D structure databases
ProteinModelPortal	Q8WWW0.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8WWW0. 26 interactions.
STRING	9606.ENSP00000347443.
PTM databases
PhosphoSite	Q8WWW0.
Polymorphism databases
DMDM	74751587.
Proteomic databases
PaxDb	Q8WWW0.
PRIDE	Q8WWW0.
Protocols and materials databases
DNASU	83593.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000304534; ENSP00000306091; ENSG00000136653. ENST00000338603; ENSP00000342620; ENSG00000136653. ENST00000355294; ENSP00000347443; ENSG00000136653. ENST00000367117; ENSP00000356084; ENSG00000136653. ENST00000577571; ENSP00000462576; ENSG00000266094. ENST00000579436; ENSP00000462099; ENSG00000266094. ENST00000580449; ENSP00000462544; ENSG00000266094. ENST00000581503; ENSP00000464039; ENSG00000266094.
GeneID	83593.
KEGG	hsa:83593.
UCSC	uc001hed.3. human. uc001hee.3. human. uc001hef.3. human.
Organism-specific databases
CTD	83593.
GeneCards	GC01P206680.
HGNC	HGNC:17609. RASSF5.
HPA	CAB022664.
MIM	607020. gene.
neXtProt	NX_Q8WWW0.
PharmGKB	PA134958571.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG308852.
HOGENOM	HOG000013025.
HOVERGEN	HBG054362.
InParanoid	Q8WWW0.
KO	K08015.
OMA	LTEYPLY.
OrthoDB	EOG4640C5.
Enzyme and pathway databases
Pathway_Interaction_DB	tcrpathway. TCR signaling in naive CD4+ T cells. cd8tcrpathway. TCR signaling in naive CD8+ T cells.
SignaLink	Q8WWW0.
Gene expression databases
ArrayExpress	Q8WWW0.
Bgee	Q8WWW0.
CleanEx	HS_RASSF5.
Genevestigator	Q8WWW0.
GermOnline	ENSG00000136653. Homo sapiens.
Family and domain databases
InterPro	IPR002219. Prot_Kinase_C-like_PE/DAG-bd. IPR000159. Ras-assoc. IPR011524. SARAH_dom. [Graphical view]
Pfam	PF00130. C1_1. 1 hit. PF00788. RA. 1 hit. [Graphical view]
SMART	SM00109. C1. 1 hit. SM00314. RA. 1 hit. [Graphical view]
PROSITE	PS50200. RA. 1 hit. PS50951. SARAH. 1 hit. PS00479. ZF_DAG_PE_1. 1 hit. PS50081. ZF_DAG_PE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	83593.
NextBio	72517.
SOURCE	Search...

Entry information

Entry name

RASF5_HUMAN

Accession

Primary (citable) accession number: Q8WWW0
Secondary accession number(s): A8K1E6 , Q5SY32, Q8WWV9, Q8WXF4, Q9BT99

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 27, 2006
Last sequence update:	March 1, 2002
Last modified:	May 29, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.